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Title: Cellular prion protein binds laminin and mediates neuritogenesis
Authors: Graner, E.
Mercadante, A. F.
Zanata, S. M.
Forlenza, O. V.
Cabral, ALB
Veiga, S. S.
Juliano, M. A.
Roesler, R.
Walz, R.
Minetti, A.
Izquierdo, I
Martins, V. R.
Brentani, R. R.
Ludwig Inst Canc Res
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Ctr Tratamento
Pesquisa Hosp Canc
Keywords: cellular prion protein
extracellular matrix
hippocampal neuron
neurite outgrowth
PC-12 cell line
Issue Date: 10-Mar-2000
Publisher: Elsevier B.V.
Citation: Molecular Brain Research. Amsterdam: Elsevier B.V., v. 76, n. 1, p. 85-92, 2000.
Abstract: Laminin (LN) plays a major role in neuronal differentiation, migration and survival. Here, we show that the cellular prion protein (PrPc) is a saturable, specific, high-affinity receptor for LN. the PrPc-LN interaction is involved in the neuritogenesis induced by NGF plus LN in the PC-12 cell line and the binding site resides in a carboxy-terminal decapeptide from the gamma-1 LN chain. Neuritogenesis induced by LN or its gamma-1-derived peptide in primary cultures from rat or either wild type or PrP null mice hippocampal neurons, indicated that PrPc is the main cellular receptor for that particular LN domain. These results point out to the importance of the PrPc-LN interaction for the neuronal plasticity mechanism. (C) 2000 Elsevier Science B.V. All rights reserved.
ISSN: 0169-328X
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